RESUMO
Interaction aspects of uranyl(VI) complexes as well as the coordinated ONNO-donor ligand with bovine serum albumin (BSA) were investigated by the fluorescence spectroscopy and computational insights. Under optimal physiological condition, it was observed that there was significant decrease in fluorescence intensity of BSA upon interaction with uranyl(VI) complexes as well as the ligand. The mechanism of interaction between the uranyl(VI) complex and BSA protein was examined by fluorescence measurement. The Stern-Volmer constant, binding affinity, binding constant, standard free energy, and fluorescence lifetime decay profile of BSA in the absence as well as in the presence of uranyl(VI) complex were determined. Furthermore, the conformational binding of uranyl(VI) complexes with BSA protein was explored via molecular docking studies, and confirmed that there is a strong affinity between the Trp-213 residue in the binding pocket of sub-domain IIA and uranyl(VI) complex.
